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Article

Conformational variability of organophosphorus hydrolase upon soman and paraoxon binding.

The journal of physical chemistry. B - 29 Dec 2011

Gomes Diego E B, Lins Roberto D, Pascutti Pedro G, Lei Chenghong, Soares Thereza A

Abstract excerpt

The bacterial enzyme organophosphorus hydrolase (OPH) exhibits both catalytic and substrate promiscuity. It hydrolyzes bonds in a variety of phosphotriester (P-O), phosphonothioate (P-S), phosphofluoridate (P-F), and phosphonocyanate (F-CN) compounds. However, its catalytic efficiency varies markedly for different substrates, limiting the broad-range application of OPH as catalyst in the bioremediation of...

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Identifiers

PMID: 22098575
DOI: 10.1021/jp208787g
PMCID: PMC3549322

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